Native Human MMP9
Cat.No. : | MMP9-30035TH |
Product Overview : | Metalloproteinase purified from cell culture media of BHK cells transfected with Murine 105 kD Gelatinase (murine homologue of Human MMP9). |
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Description : | Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. |
Tissue specificity : | Produced by normal alveolar macrophages and granulocytes. |
Form : | Liquid |
Storage buffer : | Preservative: NoneConstituents: 50% Glycerol, PBS, 250mM Sodium chloride, 0.6 % DMSO, pH 7.4 |
Storage : | Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles. |
Sequence Similarities : | Belongs to the peptidase M10A family.Contains 3 fibronectin type-II domains.Contains 4 hemopexin-like domains. |
Tag : | Non |
Gene Name : | MMP9 matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase) [ Homo sapiens ] |
Official Symbol : | MMP9 |
Synonyms : | MMP9; matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); CLG4B, matrix metalloproteinase 9 (gelatinase B, 92kD gelatinase, 92kD type IV collagenase) , matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa |
Gene ID : | 4318 |
mRNA Refseq : | NM_004994 |
Protein Refseq : | NP_004985 |
MIM : | 120361 |
Uniprot ID : | P14780 |
Chromosome Location : | 20q12-q13 |
Pathway : | Bladder cancer, organism-specific biosystem; Bladder cancer, conserved biosystem; CXCR4-mediated signaling events, organism-specific biosystem; Endochondral Ossification, organism-specific biosystem; FGF signaling pathway, organism-specific biosystem; |
Function : | collagen binding; fibronectin binding; metal ion binding; metalloendopeptidase activity; peptidase activity; |
Products Types
◆ Recombinant Protein | ||
MMP9-801H | Recombinant Human MMP9 Protein, His-tagged | +Inquiry |
MMP9-1128D | Recombinant Dog MMP9 Protein, His-tagged | +Inquiry |
MMP9-21B | Recombinant Bovine MMP9 protein(107-712aa), His-tagged | +Inquiry |
Mmp9-03M | Active Recombinant Mouse Mmp9 Protein (20-730aa), C-His-tagged | +Inquiry |
Mmp9-1132M | Recombinant Mouse Mmp9 Protein, His-tagged | +Inquiry |
◆ Native Protein | ||
MMP9-29698TH | Native Human MMP9 | +Inquiry |
MMP9-38H | Native Human MMP-9 | +Inquiry |
MMP9-9810 | Active Native Human MMP9 | +Inquiry |
◆ Lysates | ||
MMP9-2026MCL | Recombinant Mouse MMP9 cell lysate | +Inquiry |
MMP9-1940RCL | Recombinant Rat MMP9 cell lysate | +Inquiry |
MMP9-2560HCL | Recombinant Human MMP9 cell lysate | +Inquiry |
◆ Assay kits | ||
Kit-2130 | MMP-9 Inhibitor Screening Kit | +Inquiry |
Kit-3100 | MMP-9 Fluorimetric Assay Kit | +Inquiry |
Related Gene
Not For Human Consumption!
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Customer Reviews (3)
Write a reviewThe superior quality of this recombined protein has significantly enhanced the precision of our research outcomes.
Fast shipping! Ordered this product, and it arrived well-packaged and ready for use in our experiments.
Customer service went above and beyond to accommodate our specific needs, ensuring a smooth purchasing experience.
Q&As (5)
Ask a questionDysregulated MMP9 expression is associated with cancer invasion and metastasis, as it enables tumor cells to degrade the extracellular matrix and invade surrounding tissues.
Polymorphisms in the MMP9 gene can influence enzyme activity, potentially affecting the individual's susceptibility to certain diseases and the progression of pathological conditions.
MMP9 facilitates tissue remodeling by cleaving structural proteins in the extracellular matrix, such as collagen and gelatin, leading to changes in tissue architecture.
MMP9 contributes to the breakdown of the blood-brain barrier by degrading tight junction proteins, potentially exacerbating neurological disorders and neuroinflammation.
MMP9 plays a role in angiogenesis by promoting the release and activation of growth factors sequestered in the extracellular matrix, facilitating the formation of new blood vessels.
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